Identification of bacterial glycosidases in rat cecal contents.
Cecal contents of conventional and germfree rats were examined for glycosidases which may have a role in degrading glycoprotein oligosaccharides. Utilizing p-nitrophenylglycosides as substrates, we identified glycosidases in bacteria-free supernatants from cecal contents which act on beta-linkages. These cecal glycosidases appear to be of bacterial origin since: (1) direct comparisons of the enzymes in similar contents from germfree rats showed negligible activities; (2) most of the glycosidase levels in bacterial extracts were at least as high as those of soluble supernatants; and (3) disk gel electrophoresis of contents and bacterial extracts revealed in both preparations a beta-N-acetylglucosaminidase band with similar Rfs. Also, the blood group B antigenicity of germfree cecal glycoproteins was greatly decreased by conventional cecal contents. These findings indicate that beta-galactosidase and beta-N-acetylgalactosaminidase in cecal contents are bacterial in origin, and they may have a role in the bacterial catabolism of intestinal glycoproteins.
D000118:Acetylglucosaminidase / Q000378:metabolism; D000818:Animals; D001419:Bacteria / Q000201:enzymology*; D002432:Cecum / Q000201:enzymology / Q000382:microbiology*; D004589:Electrophoresis, Disc; D005856:Germ-Free Life; D006023:Glycoproteins / Q000276:immunology / Q000378:metabolism; D006026:Glycoside Hydrolases / Q000378:metabolism*; D006596:Hexosaminidases / Q000378:metabolism; D007413:Intestinal Mucosa / Q000378:metabolism; D009844:Oligosaccharides / Q000378:metabolism; D051381:Rats / Q000382:microbiology*; D001616:beta-Galactosidase / Q000378:metabolism; D048828:beta-N-Acetyl-Galactosaminidase
D006023:Glycoproteins; D009844:Oligosaccharides; D006026:Glycoside Hydrolases; D006596:Hexosaminidases; D001616:beta-Galactosidase; D000118:Acetylglucosaminidase; D048828:beta-N-Acetyl-Galactosaminidase